ID PYRC_GEOUR Reviewed; 425 AA. AC A5GF42; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 16. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=Gura_1857; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.; RT "Complete sequence of Geobacter uraniireducens Rf4."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 3/6. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000698; ABQ26047.1; -; Genomic_DNA. DR RefSeq; YP_001230620.1; -. DR GeneID; 5166201; -. DR GenomeReviews; CP000698_GR; Gura_1857. DR KEGG; gur:Gura_1857; -. DR NMPDR; fig|351605.3.peg.377; -. DR OMA; A5GF42; CDVHPVG. DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00220; -; 1. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR004722; DHOmult. DR InterPro; IPR002195; Dihydroorotase_CS. DR Pfam; PF01979; Amidohydro_1; 1. DR TIGRFAMs; TIGR00857; pyrC_multi; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Zinc. FT CHAIN 1 425 Dihydroorotase. FT /FTId=PRO_1000078107. FT METAL 61 61 Zinc 1 (By similarity). FT METAL 63 63 Zinc 1 (By similarity). FT METAL 143 143 Zinc 1; via carbamate group (By FT similarity). FT METAL 143 143 Zinc 2; via carbamate group (By FT similarity). FT METAL 180 180 Zinc 2 (By similarity). FT METAL 233 233 Zinc 2 (By similarity). FT METAL 306 306 Zinc 1 (By similarity). FT MOD_RES 143 143 N6-carboxylysine (By similarity). SQ SEQUENCE 425 AA; 44938 MW; AC06964FA760C291 CRC64; MNLLIKGGRV VDPSQNIDDT MDLLVEDGRI KEIGKGLKAP AGAEIIDAAG LLVTPGLIDM HVHLRDPGLE YKEDIVTGTR AAAAGGFTSV ACMPNTKPVN DNKAITSYIV NKAAKEALVN VFPVGSITQG SKGESLAEMG ELKESGCVAV SDDGRPVVNG ELMRRALEYA KGMGIMVISH SEELALVGEG VMNEGFTATE LGLKGIPWAA EDVAVARDVY LAEFTDSPLH IAHISTSGSV RIIRNAKARG VKVTCETAPH YFSLTDDAVR GYNTNAKMNP PLREAADVAA IKAGLADGTI DAIATDHAPH HLDEKDLEFN LALNGIVGLE TSLPLSLQLV EEGVVDLKVL LEKMTCNPAK ILGIDRGTLK VGAAADITVI DPDREWLVAA EKLASKSKNS PFIGRKMKGA AVYTVVGGKV VYKID //